極限環境微生物学会誌
Online ISSN : 1881-5758
Print ISSN : 1348-5474
ISSN-L : 1348-5474
原著論文
Purification of NADH dehydrogenase from a hyperthemophile, Pyrobaculum islandicum
M TanigawaS SekiR UetakeY Nagata
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ジャーナル フリー

2009 年 8 巻 1 号 p. 24-30

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Pyrobaculum islandicum is an ananaerobic hyperthermophilic archaeon that grows optimally at 100°C. We purified a NADH dehydrogenase from the membranes to homogeneity as analyzed by SDS-PAGE. The purified protein was suggested to comprise five subunits with molecular masses of 39 kDa, 37 kDa, 34 kDa, 31 kDa and 27 kDa, by SDS-PAGE analysis. The molecular mass of the native protein was estimated to be about 160 kDa by gel-filtration analysis. The optimal pH and temperature were 7.0 and above 80°C, respectively. The enzyme activity was shown to be highly specific to NADH, and the activity with NADPH was only 1.7% of the value with NADH.

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© 2009 Japanese Society for Extremophiles
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